{"id":{"repo_id":"utswmed","oai_identifier":"oai:utswmed-ir.tdl.org:2152.5/9626"},"canonical_url":"https://search.dev.ndltd.org/etd/utswmed/oai:utswmed-ir.tdl.org:2152.5/9626","repository":{"repo_id":"utswmed","name":"University of Texas Southwestern Medical Center","base_url":"https://utswmed-ir.tdl.org/server/oai/request"},"display":{"title":"A Novel Role for Odorant Binding Proteins in Deactivation of Drosophila Olfactory Neurons","abstract":"In insects, odorant binding proteins are a large and diverse group of low molecular weight proteins secreted into the fluid bathing olfactory and gustatory dendrites. The best-characterized OBP, known as LUSH, is required in Drosophila melanogaster for the detection of physiological levels of the male-specific pheromone cVA. While LUSH acts as a sensitizing factor for pheromone detection, the role of other OBPs encoded in the Drosophila genome is largely unknown. In an effort to characterize members of this family, I used CRISPR-Cas9 to generate and characterize a deletion of two genes encoding the homologous OBPs OS-E and OS-F. These OBPs are nearly 70% identical and their expression is restricted to a small set of antennal chemosensory sensilla. Electrophysiological analysis of the olfactory neurons within these sensilla revealed no major difference in odorant sensitivity or specificity in the mutants but did reveal a striking deactivation defect to a subset of odorants. Surprisingly, other odorants detected by the same receptor are differentially affected by the absence of OS-E and OS-F, revealing an odorant-specific role for these OBPs in deactivation kinetics. Activation kinetics remain normal for the affected odorants in mutants. Genomic rescue experiments revealed that OS-E and OS-F are also functionally redundant, as either OBP is sufficient to revert the mutant phenotype. My findings reveal a new role for OBPs in deactivation of olfactory neurons and expand our understanding of the range of OBP functions.","abstract_html":"In insects, odorant binding proteins are a large and diverse group of low molecular weight proteins secreted into the fluid bathing olfactory and gustatory dendrites. The best-characterized OBP, known as LUSH, is required in Drosophila melanogaster for the detection of physiological levels of the male-specific pheromone cVA. While LUSH acts as a sensitizing factor for pheromone detection, the role of other OBPs encoded in the Drosophila genome is largely unknown. In an effort to characterize members of this family, I used CRISPR-Cas9 to generate and characterize a deletion of two genes encoding the homologous OBPs OS-E and OS-F. These OBPs are nearly 70% identical and their expression is restricted to a small set of antennal chemosensory sensilla. Electrophysiological analysis of the olfactory neurons within these sensilla revealed no major difference in odorant sensitivity or specificity in the mutants but did reveal a striking deactivation defect to a subset of odorants. Surprisingly, other odorants detected by the same receptor are differentially affected by the absence of OS-E and OS-F, revealing an odorant-specific role for these OBPs in deactivation kinetics. Activation kinetics remain normal for the affected odorants in mutants. Genomic rescue experiments revealed that OS-E and OS-F are also functionally redundant, as either OBP is sufficient to revert the mutant phenotype. My findings reveal a new role for OBPs in deactivation of olfactory neurons and expand our understanding of the range of OBP functions.","abstract_has_math":false,"creators":["Scheuermann, Elizabeth Anne"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Meeks, Julian P.","Smith, Dean P.","Krämer, Helmut","Terman, Jonathan R."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2021,"date_issued":"2021-09-17T17:59:48Z","date_published":"2021-09-17T17:59:48Z","updated_at":"2026-07-24T05:52:31Z","subjects":["Carrier Proteins","Drosophila Proteins","Loss of Function Mutation","Phenotype"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["1268338265"],"render_values":[{"text":"1268338265","href":null,"code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/2152.5/9626","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Meeks, Julian P.","Smith, Dean P.","Krämer, Helmut","Terman, Jonathan R."]},{"key":"dc:creator","label":"Author","values":["Scheuermann, Elizabeth Anne"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2021-09-17T17:59:48Z","2019-08","2019-07-29","August 2019"]},{"key":"dc:type","label":"Dc Type","values":["Thesis","text"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Carrier Proteins","Drosophila Proteins","Loss of Function Mutation","Phenotype"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2152.5/9626","1268338265"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["In insects, odorant binding proteins are a large and diverse group of low molecular weight proteins secreted into the fluid bathing olfactory and gustatory dendrites. The best-characterized OBP, known as LUSH, is required in Drosophila melanogaster for the detection of physiological levels of the male-specific pheromone cVA. While LUSH acts as a sensitizing factor for pheromone detection, the role of other OBPs encoded in the Drosophila genome is largely unknown. In an effort to characterize members of this family, I used CRISPR-Cas9 to generate and characterize a deletion of two genes encoding the homologous OBPs OS-E and OS-F. These OBPs are nearly 70% identical and their expression is restricted to a small set of antennal chemosensory sensilla. Electrophysiological analysis of the olfactory neurons within these sensilla revealed no major difference in odorant sensitivity or specificity in the mutants but did reveal a striking deactivation defect to a subset of odorants. Surprisingly, other odorants detected by the same receptor are differentially affected by the absence of OS-E and OS-F, revealing an odorant-specific role for these OBPs in deactivation kinetics. Activation kinetics remain normal for the affected odorants in mutants. Genomic rescue experiments revealed that OS-E and OS-F are also functionally redundant, as either OBP is sufficient to revert the mutant phenotype. My findings reveal a new role for OBPs in deactivation of olfactory neurons and expand our understanding of the range of OBP functions."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["A Novel Role for Odorant Binding Proteins in Deactivation of Drosophila Olfactory Neurons"]}]}],"canonical_facts":{"dc:contributor":["Meeks, Julian P.","Smith, Dean P.","Krämer, Helmut","Terman, Jonathan R."],"dc:creator":["Scheuermann, Elizabeth Anne"],"dc:date":["2021-09-17T17:59:48Z","2019-08","2019-07-29","August 2019"],"dc:description":["In insects, odorant binding proteins are a large and diverse group of low molecular weight proteins secreted into the fluid bathing olfactory and gustatory dendrites. The best-characterized OBP, known as LUSH, is required in Drosophila melanogaster for the detection of physiological levels of the male-specific pheromone cVA. While LUSH acts as a sensitizing factor for pheromone detection, the role of other OBPs encoded in the Drosophila genome is largely unknown. In an effort to characterize members of this family, I used CRISPR-Cas9 to generate and characterize a deletion of two genes encoding the homologous OBPs OS-E and OS-F. These OBPs are nearly 70% identical and their expression is restricted to a small set of antennal chemosensory sensilla. Electrophysiological analysis of the olfactory neurons within these sensilla revealed no major difference in odorant sensitivity or specificity in the mutants but did reveal a striking deactivation defect to a subset of odorants. Surprisingly, other odorants detected by the same receptor are differentially affected by the absence of OS-E and OS-F, revealing an odorant-specific role for these OBPs in deactivation kinetics. Activation kinetics remain normal for the affected odorants in mutants. Genomic rescue experiments revealed that OS-E and OS-F are also functionally redundant, as either OBP is sufficient to revert the mutant phenotype. My findings reveal a new role for OBPs in deactivation of olfactory neurons and expand our understanding of the range of OBP functions."],"dc:format":["application/pdf"],"dc:identifier":["https://hdl.handle.net/2152.5/9626","1268338265"],"dc:language":["en"],"dc:subject":["Carrier Proteins","Drosophila Proteins","Loss of Function Mutation","Phenotype"],"dc:title":["A Novel Role for Odorant Binding Proteins in Deactivation of Drosophila Olfactory Neurons"],"dc:type":["Thesis","text"]},"updated_at":"2026-07-24T05:52:31Z"}